A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein
Post mortem biochemical staging of Alzheimer’s disease is currently based on immunochemical analysis of brain slices with the AT8 antibody. The epitope of AT8 is described around the pSer202/pThr205 region of the hyperphosphorylated form of the neuronal protein tau. In this study, NMR spectroscopy w...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal Article |
| Published: |
Wiley-VCH Verlag
2015
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| Online Access: | http://hdl.handle.net/20.500.11937/8408 |
| _version_ | 1848745650123964416 |
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| author | Gandhi, Neha Landrieu, I. Byrne, C. Kukic, P. Amniai, L. Cantrelle, F. Wieruszeski, J. Mancera, Ricardo Jacquot, Y. Lippens, G. |
| author_facet | Gandhi, Neha Landrieu, I. Byrne, C. Kukic, P. Amniai, L. Cantrelle, F. Wieruszeski, J. Mancera, Ricardo Jacquot, Y. Lippens, G. |
| author_sort | Gandhi, Neha |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Post mortem biochemical staging of Alzheimer’s disease is currently based on immunochemical analysis of brain slices with the AT8 antibody. The epitope of AT8 is described around the pSer202/pThr205 region of the hyperphosphorylated form of the neuronal protein tau. In this study, NMR spectroscopy was used to precisely map the AT8 epitope on phosphorylated tau, and derive its defining structural features by a combination of NMR analyses and molecular dynamics. A particular turn conformation is stabilized by a hydrogen bond of the phosphorylated Thr205 residue to the amide proton of Gly207, and is further stabilized by the two Arg residues opposing the pSer202/pThr205. |
| first_indexed | 2025-11-14T06:20:44Z |
| format | Journal Article |
| id | curtin-20.500.11937-8408 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T06:20:44Z |
| publishDate | 2015 |
| publisher | Wiley-VCH Verlag |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-84082017-09-13T14:35:42Z A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein Gandhi, Neha Landrieu, I. Byrne, C. Kukic, P. Amniai, L. Cantrelle, F. Wieruszeski, J. Mancera, Ricardo Jacquot, Y. Lippens, G. Post mortem biochemical staging of Alzheimer’s disease is currently based on immunochemical analysis of brain slices with the AT8 antibody. The epitope of AT8 is described around the pSer202/pThr205 region of the hyperphosphorylated form of the neuronal protein tau. In this study, NMR spectroscopy was used to precisely map the AT8 epitope on phosphorylated tau, and derive its defining structural features by a combination of NMR analyses and molecular dynamics. A particular turn conformation is stabilized by a hydrogen bond of the phosphorylated Thr205 residue to the amide proton of Gly207, and is further stabilized by the two Arg residues opposing the pSer202/pThr205. 2015 Journal Article http://hdl.handle.net/20.500.11937/8408 10.1002/anie.201501898 Wiley-VCH Verlag restricted |
| spellingShingle | Gandhi, Neha Landrieu, I. Byrne, C. Kukic, P. Amniai, L. Cantrelle, F. Wieruszeski, J. Mancera, Ricardo Jacquot, Y. Lippens, G. A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title | A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title_full | A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title_fullStr | A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title_full_unstemmed | A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title_short | A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein |
| title_sort | phosphorylation-induced turn defines the alzheimer's disease at8 antibody epitope on the tau protein |
| url | http://hdl.handle.net/20.500.11937/8408 |